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Hsp90 alpha Antibody (OASE00011)

  • Catalog#: OASE00011
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Gene Symbol:
HSP90AA1
NCBI Gene Id:
3320
Official Gene Full Name:
heat shock protein 90kDa alpha (cytosolic), class A member 1
Swissprot Id:
P07900
Protein Accession #:
NP_001017963.2
Replacement Item:
This antibody may replace item sc-1055 from Santa Cruz Biotechnology.
Host:
Mouse
Clonality:
Monoclonal
Purification:
Protein G Purified
Application:
WB, ELISA, IHC
Tissue Tool:
Find tissues and cell lines supported by DNA array analysis to express HSP90AA1.
RNA Seq:
Find tissues and cell lines supported by RNA-seq analysis to express HSP90AA1.
Immunogen:
Recombinant human Hsp90alpha; Specificity mapped to amino acids 604-731
Predicted Species Reactivity:
Human (Alpha specific)
Reconstitution and Storage:
Store at -20C. Shipping in Blue Ice or 4C.
Concentration:
1mg/mL
Datasheets/Manuals:
Printable datasheet for OASE00011
Dilution:
1ug/ml was sufficient for detection of hsp90alpha by Western Blot in 20ug of HeLa lysate.
Clone:
Hyb-K41009
Isotype:
IgG2a
Additional Information:
Background Info: Detects 90kDa proteins corresponding to the molecular mass of Hsp90alpha.
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Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively.
Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling. (7-8). The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.
In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (9).
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Certificate of Analysis: 1 ug/mL was sufficient for detection of Hsp90alpha in 20ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Storage Buffer:
PBS pH7.2, 50% glycerol
Target Reference:
1. Nemoto, T. et al. (1997) J.Biol Chem. 272, 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266, 10099-10103.
3. Arlander SJH, et al. (2003) J Biol Chem 278, 52572-52577.
4. Pearl H, et al. (2001) Adv Protein Chem 59,157-186.
5. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.
6. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133.
7. Pratt W, Toft D. (1997) Endocr Rev 18,306–360.
8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217, 420–434.
9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 8324–8328.
10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5), 881-889.

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